Abstract：
:The activation of adenosine-5'-monophosphate aminohydrolase from rabbit skeletal muscle by H+ has been demonstrated. Evidence is presented which indicates that the binding of H+ and K+ is linked, in that the dissociation constant (KA) for K+ activation is reduced as the pH is lowered. Concomitantly, the pK of several enzyme functional groups is changed when K+ is added to a solution of enzyme. This change is pK results in an uptake or release of H+, depending on the pH, and shows that K+ interacts with the enzyme to achieve its effect. The uptake or release of H+ provides a simple method of following conformational changes in the enzyme following interaction of K+. The KD for K+ interaction monitored by following pH changes is the same within experimental error as that measured from kinetic data.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Campbell JC,Suelter CHdoi
10.1021/bi00641a013subject
Has Abstractpub_date
1977-11-01 00:00:00pages
4836-9issue
22eissn
0006-2960issn
1520-4995journal_volume
16pub_type
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